View source for 4d59


==Clostridial Cysteine protease Cwp84 C116A after propeptide cleavage==
<StructureSection load='4d59' size='340' side='right'caption='[[4d59]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4d59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile_QCD-32g58 Clostridioides difficile QCD-32g58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D59 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=JEF:O-(O-(2-AMINOPROPYL)-O-(2-METHOXYETHYL)POLYPROPYLENE+GLYCOL+500)'>JEF</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4d59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d59 OCA], [https://pdbe.org/4d59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d59 RCSB], [https://www.ebi.ac.uk/pdbsum/4d59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d59 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In recent decades, the global healthcare problems caused by Clostridium difficile have increased at an alarming rate. A greater understanding of this antibiotic-resistant bacterium, particularly with respect to how it interacts with the host, is required for the development of novel strategies for fighting C. difficile infections. The surface layer (S-layer) of C. difficile is likely to be of significant importance to host-pathogen interactions. The mature S-layer is formed by a proteinaceous array consisting of multiple copies of a high-molecular-weight and a low-molecular-weight S-layer protein. These components result from the cleavage of SlpA by Cwp84, a cysteine protease. The structure of a truncated Cwp84 active-site mutant has recently been reported and the key features have been identified, providing the first structural insights into the role of Cwp84 in the formation of the S-layer. Here, two structures of Cwp84 after propeptide cleavage are presented and the three conformational changes that are observed are discussed. These changes result in a reconfiguration of the active site and exposure of the hydrophobic pocket.

Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide.,Bradshaw WJ, Roberts AK, Shone CC, Acharya KR Acta Crystallogr F Struct Biol Commun. 2015 Mar 1;71(Pt 3):295-303. doi:, 10.1107/S2053230X15001065. Epub 2015 Feb 19. PMID:25760704<ref>PMID:25760704</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4d59" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridioides difficile QCD-32g58]]
[[Category: Large Structures]]
[[Category: Acharya KR]]
[[Category: Bradshaw WJ]]
[[Category: Roberts AK]]
[[Category: Shone CC]]